Dynamics of myristoylated amino-terminal domain of Src in the plasma membrane of mechano-stimulated cells studied by single molecule imaging
| Project/Area Number |
23612002
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| Research Category |
Grant-in-Aid for Scientific Research (C)
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| Allocation Type | Multi-year Fund |
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| Section | 一般 |
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| Research Field |
Mechanobiology
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| Research Institution | Nagoya University |
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Principal Investigator |
KOBAYASHI Takeshi 名古屋大学, 医学(系)研究科(研究院), 助教 (40402565)
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| Project Period (FY) |
2011 – 2013
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| Project Status |
Completed (Fiscal Year 2013)
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| Budget Amount *help |
¥5,460,000 (Direct Cost: ¥4,200,000、Indirect Cost: ¥1,260,000)
Fiscal Year 2013: ¥1,690,000 (Direct Cost: ¥1,300,000、Indirect Cost: ¥390,000)
Fiscal Year 2012: ¥1,820,000 (Direct Cost: ¥1,400,000、Indirect Cost: ¥420,000)
Fiscal Year 2011: ¥1,950,000 (Direct Cost: ¥1,500,000、Indirect Cost: ¥450,000)
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| Keywords | シグナル伝達 / 生物物理 / １分子計測 / 1分子計測 |
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| Research Abstract |
Src is a critical signaling molecule for mechanotransduction. Mechanical stimuli applied on the cell can induce a rapid Src activation, but it remains largely unknown how mechanical stimuli activates Src molecules. Here, we observed fluorescently labeled myristoylated amino terminus of Src in the plasma membrane of living cells at the single molecule level to examine the role of lipid moiety of the amino terminus of Src on its dynamics and activation. Most probes were observed to diffuse rapidly in the membrane, but that significant fraction of the molecules exhibited temporal immobilization. We also found that the immobilization of them occurred frequently in the proximity of focal adhesions (FAs), and that it was mechano- and cholesterol-dependent. These results suggest that lipid moiety of the amino terminus of Src may play a critical role in the dynamics and activation of Src molecules around FAs through the interaction with lipid micro domains of the plasma membrane.
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Report
(4 results)
Research Products
(17 results)
